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Database: UniProt
Entry: A0A1H9SIH9_9BACI
LinkDB: A0A1H9SIH9_9BACI
Original site: A0A1H9SIH9_9BACI 
ID   A0A1H9SIH9_9BACI        Unreviewed;       511 AA.
AC   A0A1H9SIH9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:SER84767.1};
GN   ORFNames=SAMN05518872_102307 {ECO:0000313|EMBL:SER84767.1};
OS   Psychrobacillus sp. OK032.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX   NCBI_TaxID=1884358 {ECO:0000313|EMBL:SER84767.1, ECO:0000313|Proteomes:UP000199084};
RN   [1] {ECO:0000313|EMBL:SER84767.1, ECO:0000313|Proteomes:UP000199084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK032 {ECO:0000313|EMBL:SER84767.1,
RC   ECO:0000313|Proteomes:UP000199084};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000256|ARBA:ARBA00010860}.
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DR   EMBL; FOGY01000002; SER84767.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9SIH9; -.
DR   STRING; 1884358.SAMN05518872_102307; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000199084; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 4.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR017293; N-acetylmuramoyl-L-ala_amidase.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF08239; SH3_3; 4.
DR   PIRSF; PIRSF037846; Autolysin_YrvJ_prd; 2.
DR   SMART; SM00646; Ami_3; 1.
DR   SMART; SM00287; SH3b; 4.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51781; SH3B; 4.
PE   3: Inferred from homology;
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          29..91
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   DOMAIN          95..158
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   DOMAIN          173..236
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   DOMAIN          245..309
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
SQ   SEQUENCE   511 AA;  56590 MW;  04CAAA84AE62A245 CRC64;
     MKDKIVQKMT ILFLAVILLI PTIPVDAQEN EVTVNVSSLK VRTGPGLTYD TIGAVTKSDK
     LVVIDKANDW LQIKYGSTTG WVASWYTSSE AIEMTNKQIV SKVNRLNVRT EPSTSSAVIG
     QLSEGDQTPA YKSEGEWIEI DFQGRKGWVN TAYITIAEQT ANEMKSSETH TSEKLFVVSV
     DVLNIRAKAD LSSKQIGQVT KGEQFEVLDT DHNWVKVQLD NGKIGWIYSF YGTFLNEQNS
     TPSSESVNTI TILYNGTNLR SDSTTNSAVV KRADAGETFE VTDKVNDWYK VIMENQSIAY
     VASWLVSASN SVVTTDLPIQ EKKQPRKKGT LKGLSIVIDA GHGGNDRGTT GALGTDEKDI
     TLLTAELLSS KLQAAGANVI MTRQSDVYVD LRKRVSIGHQ AAADAFISLH YDAVENSTVR
     GYTTYYMHSY QKKLAEYVHA GLGSMISLRD RGTQPGNYLV LRENKQNAIL IELGYLSNPS
     EERNVTTRQF RDQATHGIYN GIINYFDNQL D
//
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